During the next year we shall continue to pursue the broad goals outlined in our specific aims, with a continuing emphasis on the determination of the amino acid sequences of certain proteins. We expect to continue or finish structural analyses of myosin light chain kinase, phosphodiesterase, a sex steroid binding protein, a protein accumulating in amyloidosis, the lectin binding and casein kinase II. In each case, the structural data is expected to provide either new information about the domain substructure and probable origin of the protein or new insights into the function of the protein in healthy or diseased tissue. We shall continue to examine the chemical nature of profilaggrin, the very large, multidomain, precursor of a keratin assembling protein in differentiating epidermis. Three of the proteins under study are regulated by calcium and calmodulin (phosphodiesterase, myosin light chain kinase, and the Gamma chain of phosphorylase kinase). We plan to identify common features of the calmodulin docking sites and attempt to understand how that interaction modulates the activity of the interacting protein. Finally, we plan to continue to study the covalent processing events associated with the maturation or regulation of proteins during or after translation--particularly myristylation and phosphorylation.